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Database: UniProt
Entry: A0A3B7M4Q3_9GAMM
LinkDB: A0A3B7M4Q3_9GAMM
Original site: A0A3B7M4Q3_9GAMM 
ID   A0A3B7M4Q3_9GAMM        Unreviewed;      1155 AA.
AC   A0A3B7M4Q3;
DT   16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT   16-JAN-2019, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=Transcription-repair-coupling factor {ECO:0000256|HAMAP-Rule:MF_00969};
DE            Short=TRCF {ECO:0000256|HAMAP-Rule:MF_00969};
DE            EC=3.6.4.- {ECO:0000256|HAMAP-Rule:MF_00969};
GN   Name=mfd {ECO:0000256|HAMAP-Rule:MF_00969};
GN   ORFNames=CDG61_09705 {ECO:0000313|EMBL:AXY60272.1};
OS   Acinetobacter sp. WCHAc010052.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=2004647 {ECO:0000313|EMBL:AXY60272.1, ECO:0000313|Proteomes:UP000264387};
RN   [1] {ECO:0000313|EMBL:AXY60272.1, ECO:0000313|Proteomes:UP000264387}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WCHAc010052 {ECO:0000313|EMBL:AXY60272.1,
RC   ECO:0000313|Proteomes:UP000264387};
RA   Hu Y., Long H., Feng Y., Zong Z.;
RT   "The complete genome of Acinetobacter sp. strain WCHAc010052.";
RL   Submitted (SEP-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Couples transcription and DNA repair by recognizing RNA
CC       polymerase (RNAP) stalled at DNA lesions. Mediates ATP-dependent
CC       release of RNAP and its truncated transcript from the DNA, and
CC       recruitment of nucleotide excision repair machinery to the damaged
CC       site. {ECO:0000256|HAMAP-Rule:MF_00969}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00969}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the helicase family.
CC       RecG subfamily. {ECO:0000256|HAMAP-Rule:MF_00969}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the UvrB family.
CC       {ECO:0000256|HAMAP-Rule:MF_00969}.
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DR   EMBL; CP032143; AXY60272.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3B7M4Q3; -.
DR   OrthoDB; 9804325at2; -.
DR   Proteomes; UP000264387; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003684; F:damaged DNA binding; IEA:InterPro.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:UniProtKB-UniRule.
DR   GO; GO:0000716; P:transcription-coupled nucleotide-excision repair, DNA damage recognition; IEA:UniProtKB-UniRule.
DR   CDD; cd17991; DEXHc_TRCF; 1.
DR   Gene3D; 2.40.10.170; -; 1.
DR   Gene3D; 3.40.50.11140; -; 1.
DR   Gene3D; 3.40.50.11180; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   Gene3D; 3.30.2060.10; Penicillin-binding protein 1b domain; 1.
DR   Gene3D; 3.90.1150.50; Transcription-repair-coupling factor, D7 domain; 1.
DR   HAMAP; MF_00969; TRCF; 1.
DR   InterPro; IPR003711; CarD-like/TRCF_RID.
DR   InterPro; IPR036101; CarD-like/TRCF_RID_sf.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR004576; Mfd.
DR   InterPro; IPR048635; MFD_D3.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR047112; RecG/Mfd.
DR   InterPro; IPR037235; TRCF-like_C_D7.
DR   InterPro; IPR005118; TRCF_C.
DR   InterPro; IPR041471; UvrB_inter.
DR   NCBIfam; TIGR00580; mfd; 1.
DR   PANTHER; PTHR47964; ATP-DEPENDENT DNA HELICASE HOMOLOG RECG, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR47964:SF1; ATP-DEPENDENT DNA HELICASE HOMOLOG RECG, CHLOROPLASTIC; 1.
DR   Pfam; PF02559; CarD_TRCF_RID; 1.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF21132; MFD_D3; 1.
DR   Pfam; PF03461; TRCF; 1.
DR   Pfam; PF17757; UvrB_inter; 1.
DR   SMART; SM01058; CarD_TRCF; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SMART; SM00982; TRCF; 1.
DR   SUPFAM; SSF141259; CarD-like; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 3.
DR   SUPFAM; SSF143517; TRCF domain-like; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00969}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00969};
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|HAMAP-
KW   Rule:MF_00969};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|HAMAP-
KW   Rule:MF_00969};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW   Rule:MF_00969}; Helicase {ECO:0000256|ARBA:ARBA00022806};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00969};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00969}.
FT   DOMAIN          620..781
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          803..956
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
SQ   SEQUENCE   1155 AA;  130622 MW;  AD05BAD02AD44B61 CRC64;
     MFTQEISELN LKQLKAGEKR WIGSMLGSSA ALLFKEISEK SSQLFVLVAR NNQHLGQLES
     ELEFYGIKPT IFPDWEILPY DRLSPHQDIV SERLSILSNM PQSGILLVSA TTLAQRVAPT
     SWVLGEHFDI KIGQTFDLEQ QKLRLIQAGY HLVDTVYDHG EFAVRGSIMD IYASGQDAPI
     RIDLFDNEID TLKFFDPETQ RTTTKIESFT VLPAKEFPLK EARSTFRDRY AESFPTANPK
     KNPIYQDVME GIASPGLDFY FPLFFSAEAM QTQSSLISYL PGNAVVITDK HLEDGLTSFW
     KDVMRRYEDR RHNVDQPLLP PEQIFLQPNQ IFEFLNQFPR IIADTEVVEI RSGALNLSAE
     LPPRLAVDPK QEKPFSAVKK YIDDANHPVL LVAESAGRRE TLKDALCPTL GEIPVVSNFA
     EFQQSHFSVA ITNAPLDRGL VITDHLSVIS ENQLYEHRVV QRRRKRQHEV SEEFLVRSLT
     ELSIGAPVVH IDHGVGRYAG LITLNIDDQD YEFLQLNYAD EAKVYVPVTN LHLISRFSGG
     DPDLAPLHKL GTDAWNKAKR KALEQIHDVA AELLHIQARR QAKPGISFEL EQSSYMQFSS
     GFAYEETLDQ ANAIEATLYD MQLAKPMDRL VCGDVGFGKT EVAMRAAFVA VQNNKQVAVL
     VPTTLLAQQH YESFKDRFAD WPIRIEVLSR FGTSKAHTRT IEDLADGKVD IVIGTHKILQ
     ENIQFKNLGL MIVDEEHRFG VRDKERIKAM RADVDMLTLT ATPIPRTLNM AFSGMRDLSI
     IATPPARRLA VKTFVNEQTD ETMKEAILRE LLRGGQVYIL HNEVDTIERA AENIRNLVPE
     ARVAVAHGQM RERELEQVMQ QFYHKEFNVL VCSTIIETGI DVPNANTIII ERADKLGLAQ
     LHQLRGRVGR SHHQAYAYLM VPSIKGLKGD AEKRLDAISR ASTLGAGFML ATEDLEIRGA
     GELLGEQQSG SMQAIGYSLY MEMLEKATKA IQNGKTPNFD APLSLTAEIN LHMPALIPDE
     YLGDVHQRLM FYKRISNANT QEKLDHIRME LIDRFGVPPV QVKQLFSVHQ IRIIAEKLEI
     TKIDLSANGG SIEFSPDTPV QAITIIQMMQ KHPTWFRMEG GQRLRVMVMM EEYEKRIRFI
     SDLLNSLVSE SGLKP
//
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